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Q9C141 (DMAW2_CLAPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tryptophan dimethylallyltransferase 2

EC=2.5.1.34
Alternative name(s):
4-dimethylallyltryptophan synthase 2
All-trans-hexaprenyl-diphosphate synthase 2
L-tryptophan dimethylallyl transferase 2
Short name=DMATS 2
Gene names
Name:dmaW2
Synonyms:cpd2
OrganismClaviceps purpurea (Ergot fungus) (Sphacelia purpurea)
Taxonomic identifier5111 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeClaviceps

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the first step of ergot alkaloid biosynthesis. Ergot alkaloids, which are produced by endophyte fungi, can enhance plant host fitness, but also cause livestock toxicosis to host plants By similarity.

Catalytic activity

Dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan.

Pathway

Alkaloid biosynthesis; ergot alkaloid biosynthesis.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the tryptophan dimethylallyltransferase family.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Molecular functionTransferase
Gene Ontology (GO)
   Biological processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontryptophan dimethylallyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Tryptophan dimethylallyltransferase 2
PRO_0000181365

Sequences

Sequence LengthMass (Da)Tools
Q9C141 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1ED9FE8900810E59

FASTA44851,521
        10         20         30         40         50         60 
MSTAKDPGNG VYEILSLIFD FPSNEQRLWW HSTAPMFAAM LDNAGYSVHD QYRHLSIFKT 

        70         80         90        100        110        120 
HIIPFLGVYP TKGQERWLSI LTRCGLPLEL SLNCTDSVVR YAYEPINEMT GTEKDPSNTL 

       130        140        150        160        170        180 
PIIGSVQKLA QIQAGIDLEW FSYFKDELTL DESESAILQD TELVKEQIKT QNKLALDLKE 

       190        200        210        220        230        240 
SQFALKVYFY PHLKSIATGN STHFLIFDSV FKLSQKHDSI QPAFQALCDY VSRRNDSSEV 

       250        260        270        280        290        300 
DQHRALHARL LSCDLIDPAK SRVKIYLQEQ TVSLPAMEDL WTLGGRRVDA STMDGLDMLR 

       310        320        330        340        350        360 
ELWSLLKVPT GHLEYPKGYM ELGEIPNEQL PSLVNYTLHR NDPMPEPQVY FTVFGMNDAE 

       370        380        390        400        410        420 
ISNALTIFLQ RHGFADMAKK YRVFLQDSYP YHDFESLNYL HSLVSFSYRR NKPYLSVYLH 

       430        440 
TFETGRWPVV ADSPISFDAY RRCDLSTK 

« Hide

References

[1]"Molecular analysis of dimethyl-allyl-tryptophan-synthase-genes."
Arntz C., Tudzynski P.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: T5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ312753 Genomic DNA. Translation: CAC37396.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017795. Aromatic_prenylTrfase_DMATS.
IPR012148. Trp_dimethylallyltransferase.
IPR017796. Trp_dimethylallylTrfase_sub.
[Graphical view]
PfamPF11991. Trp_DMAT. 1 hit.
[Graphical view]
PIRSFPIRSF000509. Trp_DMAT. 1 hit.
TIGRFAMsTIGR03429. Arom_pren_DMATS. 1 hit.
TIGR03430. Trp_dimet_allyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDMAW2_CLAPU
AccessionPrimary (citable) accession number: Q9C141
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: October 19, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families